Cited by 895Metal-Catalyzed Oxygenation MechanismsGlutathione Transferases and PolymorphismsRedox biology and oxidative stress

The DOI matches its Crossref record, with a small difference in title or year; 38 of the 38 references it cites were found in a registry or an index.

Superoxide Dismutase

Open access

Weisiger, Richard A., Fridovich, Irwin·1973·Journal of Biological Chemistry

DOI 10.1016/s0021-9258(19)43969-0

Open this paper in CoChat — free account

Abstract

Abstract Fresh chicken liver contains two types of superoxide dismutase, one of which is localized in the mitochondria while the other is found in the cytosol. The mitochondrial superoxide dismutase was inactivated by treatment with mixtures of chloroform and ethanol whereas the cytosol superoxide dismutase was not. The cytosol superoxide dismutase was inhibited by cyanide, whereas the mitochondrial enzyme was not. The cytosol superoxide dismutase was purified to homogeneity and was found to contain copper and zinc and to be similar to the other cupro-zinc superoxide dismutases which have been isolated from diverse eukaryotes. In contrast, the superoxide dismutase present in chicken liver mitochondria, when isolated, was found to a manganoprotein which has a molecular weight of 80,000. It is composed of four subunits of equal size, which are not covalently joined. It contains 2.3 atoms of manganese per molecule and is strikingly similar to the superoxide dismutase previously isolated from bacteria (Keele, B. B., Jr., McCord, J. M., and Fridovich, I. (1970) J. Biol. Chem. 245, 6176–6181; Vance, P. G., Keele, B. B., Jr., and Rajagopalan, K. V. (1972) J. Biol. Chem. 247, 4782–4786). Avimanganin which was isolated from chicken liver mitochondria (Scrutton, M. C. (1971) Biochemistry 10, 3897–3905) appears to be an inactive form of mitochondrial superoxide dismutase. The similarity between the mitochondrial superoxide dismutase and the corresponding enzymes from Escherichia coli and from Streptococcus mutans and the marked dissimilarity to the superoxide dismutase found in the cytosols of eukaryotes lends support to the theory that mitochondria have evolved from aerobic prokaryotes, which entered into an endocellular symbiosis with a protoeukaryote. Chicken liver was not unique in possessing distinct superoxide dismutases in cytosol and in mitochondrial compartments, since the same situation was shown to occur in pig heart. The chicken liver cytosol superoxide dismutase exhibited two peculiar properties. Thus when stored in deep, concentrated solutions it underwent autoreduction to a yellow cuprous form which retained enzymatic activity, and it polymerized to forms which likewise retained activity. Both of these changes were reversible and appeared to be due to reactive sulfhydryl groups which could act as the endogenous reductant and could form intermolecular disulfide bridges. The cytosol superoxide dismutase consisted of a family of electrophoretically distinct forms which could readily be separated on a preparative scale by isoelectric focusing. These multiple forms were indistinguishable in size and in specific activity. The chemical basis of these differences in charge was not explored.

Integrity signals

Registry

Crossref · 10.1016/s0021-9258(19)43969-0

Cites

38 of 38 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis.
Weber, K., & Osborn, M. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94333-4 · Cited by 16,688
DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS *
Davis, B. J. (1964) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1964.tb14213.x · Cited by 16,129
Superoxide Dismutase
McCord, J. M., & Fridovich, I. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63504-5 · Cited by 12,952
Self-citation
Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels
Beauchamp, C., & Fridovich, I. (1971) · Analytical Biochemistry · doi:10.1016/0003-2697(71)90370-8 · Cited by 12,892
Self-citation
Spectroscopic Determination of Tryptophan and Tyrosine in Proteins *
Edelhoch, H. (1967) · Biochemistry · doi:10.1021/bi00859a010 · Cited by 3,438
Equilibrium Ultracentrifugation of Dilute Solutions*
Yphantis, D. A. (1964) · Biochemistry · doi:10.1021/bi00891a003 · Cited by 3,386
High resolution acrylamide gel electrophoresis of histones
Panyim, S., & Chalkley, R. G. (1969) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(69)90042-3 · Cited by 2,459
THE OXIDATION OF RIBONUCLEASE WITH PERFORMIC ACID
Hirs, C. H. W. (1956) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)65721-7 · Cited by 1,862
ORIGIN OF EUKARYOTIC CELLS
Raven, P. H., & Margulis, L. (1971) · Evolution · doi:10.1111/j.1558-5646.1971.tb01930.x · Cited by 1,483
An Enzyme-Based Theory of Obligate Anaerobiosis: The Physiological Function of Superoxide Dismutase
McCord, J. M., Keele, B. B., & Fridovich, I. (1971) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.68.5.1024 · Cited by 976
Self-citation

Show all 37 references

Research works printed but not linked: 4

Tsuchihashi, 1923, Biochem. Z., 140, 63
Cohen, 1970, Amer. Sci., 58, 281
Schnepf, 1972, 2, 299
Dixon, 1935, Proc. Roy. Soc. Ser. B Biol. Sci., 119, 159

Sorted by citations

Items 101–200 of 895

Mutant SOD1 in neuronal mitochondria causes toxicity and mitochondrial dynamics abnormalities
Magrané, J., Hervías, I., Henning, M. S., Damiano, M. G., Kawamata, H., & Manfredi, G. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp421 · Cited by 171
The Role of Reactive Oxygen Species in the Life Cycle of the Mitochondrion
Venditti, P., & Meo, S. D. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21062173 · Cited by 176
Radiation modulation of MicroRNA in prostate cancer cell lines
Josson, S., Sung, S., Lao, K., Chung, L. W. K., & Johnstone, P. A. S. (2008) · The Prostate · doi:10.1002/pros.20827 · Cited by 172
The role of manganese in photosynthetic oxygen evolution
Amesz, J. (1983) · Biochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics · doi:10.1016/0304-4173(83)90008-3 · Cited by 169
Superoxide Dismutase and Oxygen Toxicity in a Eukaryote
Gregory, E. M., Goscin, S. A., & Fridovich, I. (1974) · Journal of Bacteriology · doi:10.1128/jb.117.2.456-460.1974 · Cited by 168
Self-citation
Isolation of a new copper — Containing superoxide dismutase bacteriocuprein
Puget, K., & Michelson, A. M. (1974) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(74)80492-4 · Cited by 167
On the Origin of Superoxide Dismutase: An Evolutionary Perspective of Superoxide-Mediated Redox Signaling
Case, A. J. (2017) · Antioxidants · doi:10.3390/antiox6040082 · Cited by 168
Graduate Theses and Dissertations
Davis, M., Davis, K. J., & Dunagan, M. M. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-384727-0.00006-9 · Cited by 165
Blocking NMDA receptors prevents the oxidative stress induced by acute ammonia intoxication
Kosenko, E. A., Kaminski, Y., Lopata, O., Muravyov, N., & Felipo, V. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00339-6 · Cited by 163
The Nature of Antioxidant Defense Mechanisms: A Lesson from Transgenic Studies
Ho, Y., Magnenat, J.-L., Gargano, M. D., & Cao, J. (1998) · Environmental Health Perspectives · doi:10.1289/ehp.98106s51219 · Cited by 171
Modulation of rat liver mitochondrial antioxidant defence system by thyroid hormone
Das, K., & Chainy, G. B. N. (2001) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(01)00048-5 · Cited by 160
Enhancement of reactive oxygen-dependent mitochondrial membrane lipid peroxidation by the anticancer drug adriamycin
Mimnaugh, E. G., Trush, M. A., Bhatnagar, M., & Gram, T. E. (1985) · Biochemical Pharmacology · doi:10.1016/0006-2952(85)90766-x · Cited by 159
Amyotrophic Lateral Sclerosis: From Current Developments in the Laboratory to Clinical Implications
Cozzolino, M., Ferri, A., & Teresa Carrì, M. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.1760 · Cited by 156
Mitochondrial nitric oxide synthase
Brookes, P. S. (2003) · Mitochondrion · doi:10.1016/j.mito.2003.10.001 · Cited by 157
Oxidative Stress in Airways: Is There a Role for Extracellular Superoxide Dismutase?
Bowler, R. P., & Crapo, J. D. (2002) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.2206014 · Cited by 157
Inhibition of superoxide dismutases by azide
Misra, H. P., & Fridovich, I. (1978) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(78)90218-7 · Cited by 154
Self-citation
Subcellular localization of superoxide dismutase in rat liver
Peeters-Joris, C., Am, V., & Baudhuin, P. (1975) · Biochemical Journal · doi:10.1042/bj1500031 · Cited by 154
The Role of Oxidative Stress in Chronic Obstructive Pulmonary Disease
Bowler, R. P., Barnes, P. J., & Crapo, J. D. (2004) · COPD Journal of Chronic Obstructive Pulmonary Disease · doi:10.1081/copd-200027031 · Cited by 153
Oxidative Stress, Mitochondrial Dysfunction, and Epilepsy
Patel, M. N. (2002) · Free Radical Research · doi:10.1080/1071576021000016391 · Cited by 152
Redox dynamics of manganese as a mitochondrial life-death switch
Smith, M. R., Fernandes, J., Go, Y., & Jones, D. P. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.10.126 · Cited by 152
Mitochondrial Localization of Superoxide Dismutase is Required for Decreasing Radiation-Induced Cellular Damage
Epperly, M. W., Gretton, J. E., Sikora, C. A., Jefferson, M., Bernarding, M., Nie, S., & Greenberger, J. S. (2003) · Radiation Research · doi:10.1667/rr3081 · Cited by 150
Localization of superoxide dismutases in Alzheimer's disease and Down's syndrome neocortex and hippocampus.
Furuta, A., Price, D. L., Pardo, C. A., Troncoso, J. C., Xu, Z., Taniguchi, N., & Martin, L. J. (1995) · Europe PMC (PubMed Central) · Cited by 151
Redox chemistry of dioxygen species
Wilshire, J. P., & Sawyer, D. T. (1979) · Accounts of Chemical Research · doi:10.1021/ar50135a005 · Cited by 148
Oxygen and the copper chaperone CCS regulate posttranslational activation of Cu,Zn superoxide dismutase
Brown, N. M., Torres, A. S., Doan, P. E., & O’Halloran, T. V. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401175101 · Cited by 148
Heat Shock Protein 72 Enhances Manganese Superoxide Dismutase Activity During Myocardial Ischemia-Reperfusion Injury, Associated With Mitochondrial Protection and Apoptosis Reduction
Suzuki, K., Murtuza, B., Sammut, I. A., Latif, N., Jayakumar, J., Smolenski, R. T., Kaneda, Y., Sawa, Y., Matsuda, H., & Yacoub, M. H. (2002) · Circulation · doi:10.1161/01.cir.0000032880.55215.92 · Cited by 147
Mitochondrial oxidative stress and the metabolic syndrome
James, A. M., Collins, Y., Logan, A., & Murphy, M. P. (2012) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2012.06.008 · Cited by 150
Mitochondrial Dysfunction, Oxidative Stress, and Therapeutic Strategies in Diabetes, Obesity, and Cardiovascular Disease
Cojocaru, K.-A., Luchian, I. A., Goriuc, A., Antoci, L.-M., Ciobanu, C.-G., Popescu, R. M., Vlad, C.-E., Blaj, M., & Foia, L. G. (2023) · Antioxidants · doi:10.3390/antiox12030658 · Cited by 160
Trace Elements in the Fetus and Young Infant
SHAW, J. C. L. (1979) · American journal of diseases of children · doi:10.1001/archpedi.1979.02130120052011 · Cited by 145
Isolation and characterization of complementary DNAs encoding human manganese‐containing superoxide dismutase
Ho, Y., & Crapo, J. D. (1988) · FEBS Letters · doi:10.1016/0014-5793(88)81136-0 · Cited by 143
Brassinolide alleviates salt stress and increases antioxidant activity of cowpea plants (Vigna sinensis)
El-Mashad, A. A. A., & Mohamed, H. I. (2011) · PROTOPLASMA · doi:10.1007/s00709-011-0300-7 · Cited by 142
Superoxide dismutase and neurological disorders
Chidambaram, S. B., Anand, N., Varma, S. R., Ramamurthy, S., Vichitra, C., Sharma, A., Mahalakshmi, A. M., & Essa, M. M. (2024) · IBRO Neuroscience Reports · doi:10.1016/j.ibneur.2023.11.007 · Cited by 162
Properties of spermatozoal superoxide dismutase and lack of involvement of superoxides in metal-ion-catalysed lipid-peroxidation and reactions in semen
Mennella, M. R. F., & Jones, R. (1980) · Biochemical Journal · doi:10.1042/bj1910289 · Cited by 140
Subcellular Localisation and Identification of Superoxide Dismutase in the Leaves of Higher Plants
JACKSON, C., Dench, J. E., Moore, A. L., Halliwell, B. B., Foyer, C. H., & Hall, D. O. (1978) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1978.tb12685.x · Cited by 140
Mitochondria and arrhythmias
Yang, K., Bonini, M. G., & Dudley, S. C. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.03.033 · Cited by 139
Anti-oxidative effects of superoxide dismutase 3 on inflammatory diseases
Nguyen, N. H., Tran, G., & Nguyen, C. T. (2019) · Journal of Molecular Medicine · doi:10.1007/s00109-019-01845-2 · Cited by 142
The Role of Reactive Oxygen Species in Acute Myeloid Leukaemia
Sillar, J. R., Germon, Z. P., Iuliis, G. N. D., & Dun, M. D. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20236003 · Cited by 139
Induction of superoxide dismutase by oxygen in neonatal rat lung.
Stevens, J. B., & Autor, A. P. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)40420-0 · Cited by 138
Hypothesis: the mitochondrial NO(*) signaling pathway, and the transduction of nitrosative to oxidative cell signals: an alternative function for cytochrome c oxidase
Brookes, P., & Darley-Usmar, V. M. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00805-x · Cited by 137
A role for divalent metal transporter (DMT1) in mitochondrial uptake of iron and manganese
Wolff, N. A., Garrick, M. D., Zhao, L., Garrick, L. M., Ghio, A. J., & Thévenod, F. (2018) · Scientific Reports · doi:10.1038/s41598-017-18584-4 · Cited by 134
Reactive Oxygen and Nitrogen Species: Impact on Endothelial Dysfunction
Salisbury, D., & Bronas, U. (2015) · Nursing Research · doi:10.1097/nnr.0000000000000068 · Cited by 134
Age-related changes in antioxidant enzyme activities are region and organ, as well as sex, selective in the rat
Carrillo, M.-C., Kanai, S., Sato, Y., & Kitani, K. (1992) · Mechanisms of Ageing and Development · doi:10.1016/0047-6374(92)90035-c · Cited by 134
Visualization of catalase on acrylamide gels
Gregory, E. M., & Fridovich, I. (1974) · Analytical Biochemistry · doi:10.1016/0003-2697(74)90440-0 · Cited by 134
Self-citation
Hemes, Chlorophylls, and Related Compounds: Biosynthesis and Metabolic Regulation
Granick, S., & Beale, S. I. (1978) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470122914.ch2 · Cited by 133
Exploiting Oxidative Microenvironments in the Body as Triggers for Drug Delivery Systems
Joshi-Barr, S., Lux, C. D. G., Mahmoud, E., & Almutairi, A. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5754 · Cited by 134
Manganese(II) catalyzes the bicarbonate-dependent oxidation of amino acids by hydrogen peroxide and the amino acid-facilitated dismutation of hydrogen peroxide.
Berlett, B. S., Chock, P. B., Yim, M. B., & Stadtman, E. R. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.1.389 · Cited by 132
Molecular Structure of a Functional Rat Gene for Manganese-containing Superoxide Dismutase
Ho, Y., Howard, A. J., & Crapo, J. D. (1991) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb/4.3.278 · Cited by 131
Iron containing superoxide dismutases from luminous bacteria
Puget, K., & Michelson, A. M. (1974) · Biochimie · doi:10.1016/s0300-9084(74)80019-2 · Cited by 131
Production of Superoxide and Activity of Superoxide Dismutase in Rabbit Epididymal Spermatozoa
Holland, M. K., Álvarez, J. G., & Storey, B. T. (1982) · Biology of Reproduction · doi:10.1095/biolreprod27.5.1109 · Cited by 129
1-Methyl-4-phenylpyridinium (MPP+)-induced apoptosis and mitochondrial oxidant generation: role of transferrin-receptor-dependent iron and hydrogen peroxide
Kalivendi, S. V., Kotamraju, S., CUNNINGHAM, S., Shang, T., Hillard, C. J., & Kalyanaraman, B. (2003) · Biochemical Journal · doi:10.1042/bj20021525 · Cited by 128
Mechanisms of Sudden Cardiac Death: Oxidants and Metabolism
Yang, K.-C., Kyle, J. W., Makielski, J. C., & Dudley, S. C. (2015) · Circulation Research · doi:10.1161/circresaha.116.304691 · Cited by 127
Mitochondrial Function, Morphology, and Axonal Transport in Amyotrophic Lateral Sclerosis
Magrané, J., & Manfredi, G. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2604 · Cited by 127
Proteomics of buccal squamous cell carcinoma: The involvement of multiple pathways in tumorigenesis
Chen, J., He, Q., Yuen, A. P. W., & Chiu, J. (2004) · PROTEOMICS · doi:10.1002/pmic.200300762 · Cited by 127
Expression of manganese superoxide dismutase promotes cellular differentiation
Clair, D. K. S., Oberley, T. D., Muse, K. E., & Clair, W. H. S. (1994) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(94)90153-8 · Cited by 127
Copper-Containing Oxidases and Superoxide Dismutase
Malmström, B. G., Andréasson, L., & Reinhammar, B. (1975) · The Enzymes · doi:10.1016/s1874-6047(08)60231-0 · Cited by 126
Prospects for therapeutic mitochondrial transplantation
Gollihue, J. L., & Rabchevsky, A. G. (2017) · Mitochondrion · doi:10.1016/j.mito.2017.05.007 · Cited by 125
The Physiology of Obligate Anaerobiosis
Morris, J. (1975) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/s0065-2911(08)60282-9 · Cited by 118
Superoxide dismutase: “Positive” spectrophotometric assays
Misra, H. P., & Fridovich, I. (1977) · Analytical Biochemistry · doi:10.1016/0003-2697(77)90429-8 · Cited by 122
Self-citation
Role of superoxide radical in mitochondrial dehydrogenase reactions
Forman, H. J., & Kennedy, J. A. (1974) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(74)90418-5 · Cited by 122
Chemotactic factor‐induced generation of superoxide radicals by human neutrophils
Simchowitz, L., Mehta, J., & Spilberg, I. (1979) · Arthritis & Rheumatism · doi:10.1002/art.1780220711 · Cited by 121
Superoxide dismutase in various tissues from rabbits bearing the Vx-2 carcinoma in the maxillary sinus.
Takada, Y., Noguchi, T., Okabe, T., & Kajiyama, M. (1982) · PubMed · Cited by 119
Enhanced mitochondrial superoxide in hyperglycemic endothelial cells: direct measurements and formation of hydrogen peroxide and peroxynitrite
Quijano, C., Castro, L., Peluffo, G., Valez, V., & Radí, R. (2007) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00761.2007 · Cited by 120
Isolation and characterization of the cytosolic and mitochondrial superoxide dismutases of maize
Baum, J. A., & Scandalios, J. G. (1981) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(81)90089-8 · Cited by 117
Raw material enzymatic activity determination: A specific case for validation and comparison of analytical methods—The example of superoxide dismutase (SOD)
Zhou, J. Y., & Prognon, P. (2005) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2005.09.022 · Cited by 116
The Credible Role of Curcumin in Oxidative Stress-Mediated Mitochondrial Dysfunction in Mammals
Sathyabhama, M., Dharshini, L. C. P., Karthikeyan, A., Senthil, K., & Min, T. (2022) · Biomolecules · doi:10.3390/biom12101405 · Cited by 120
Induction of Several Antioxidant Enzymes in the Selection of a Salt-Tolerant Cell Line of Pisum sativum
Olmos, E., Hernández, J. A., Sevilla, F., & Hellín, E. (1994) · Journal of Plant Physiology · doi:10.1016/s0176-1617(11)82142-5 · Cited by 115
Immunolocalization of four antioxidant enzymes in digestive glands of mollusks and crustaceans and fish liver
Orbea, A., Fahimi, H. D., & Cajaraville, M. P. (2000) · Histochemistry and Cell Biology · doi:10.1007/s004180000207 · Cited by 115
Superoxide Dismutase Activity in Leukocytes
DeChatelet, L. R., McCall, C. E., McPhail, L. C., & Johnston, R. B. (1974) · Journal of Clinical Investigation · doi:10.1172/jci107659 · Cited by 114
Cabbage looper antioxidant enzymes: Tissue specificity
Ahmad, S., Duval, D. L., Weinhold, L. C., & Pardini, R. S. (1991) · Insect Biochemistry · doi:10.1016/0020-1790(91)90111-q · Cited by 114
Regulation of Superoxide Dismutase Activity by Dietary Manganese
de Rosa, G., Keen, C. L., Leach, R. M., & Hurley, L. S. (1980) · Journal of Nutrition · doi:10.1093/jn/110.4.795 · Cited by 114
Localization of manganese superoxide dismutase in peroxisomes isolated from Pisum sativum L.
Sandalio, L. M., Palma, J. M., & del Río, L. A. (1987) · Plant Science · doi:10.1016/0168-9452(87)90213-5 · Cited by 114
Evidence for widespread, severe brain copper deficiency in Alzheimer's dementia
Xu, J., Church, S. J., Patassini, S., Begley, P., Waldvogel, H. J., Curtis, M. A., Faull, R. L. M., Unwin, R. D., & Cooper, G. J. S. (2017) · Metallomics · doi:10.1039/c7mt00074j · Cited by 113
Binding and Nuclear Relocalization of Protein Kinase R by Human Cytomegalovirus TRS1
Hakki, M., Marshall, E. E., Niro, K. L. D., & Geballe, A. P. (2006) · Journal of Virology · doi:10.1128/jvi.00957-06 · Cited by 112
A spectrophotometric assay for superoxide dismutase activities in crude tissue fractions
Kuthan, H., Haussmann, H.-J., & Werringloer, J. (1986) · Biochemical Journal · doi:10.1042/bj2370175 · Cited by 111
Immunocytochemical evidence for a peroxisomal localization of manganese superoxide dismutase in leaf protoplasts from a higher plant
del Río, L. A., Lyon, D. S., Oláh, I., Glick, B., & Salin, M. L. (1983) · Planta · doi:10.1007/bf01075257 · Cited by 111
Clinical Significances of Superoxide Dismutases: Changes in Aging, Diabetes, Ischemia, and Cancer
Taniguchi, N. (1992) · Advances in clinical chemistry · doi:10.1016/s0065-2423(08)60221-8 · Cited by 111
The polymorphism of manganese superoxide dismutase is associated with diabetic nephropathy in Japanese type 2 diabetic patients
Nomiyama, T., Tanaka, Y., Piao, L., Nagasaka, K., Sakai, K., Ogihara, T., Nakajima, K., Watada, H., & Kawamori, R. (2003) · Journal of Human Genetics · doi:10.1007/s100380300021 · Cited by 110
Bacteriocuprein superoxide dismutases in pseudomonads
Steinman, H. M. (1985) · Journal of Bacteriology · doi:10.1128/jb.162.3.1255-1260.1985 · Cited by 109
Chemical modification of arginine at the active site of the bovine erythrocyte superoxide dismutase
Malinowski, D. P., & Fridovich, I. (1979) · Biochemistry · doi:10.1021/bi00593a023 · Cited by 108
Self-citation
Dual Role of Reactive Oxygen Species in Muscle Function: Can Antioxidant Dietary Supplements Counteract Age-Related Sarcopenia?
Damiano, S., Muscariello, E., Rosa, G. L., Maro, M. D., Mondola, P., & Santillo, M. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20153815 · Cited by 116
Changes in Activity of the Manganese Superoxide Dismutase Enzyme in Tissues of the Rat with Changes in Dietary Manganese
Paynter, D. I. (1980) · Journal of Nutrition · doi:10.1093/jn/110.3.437 · Cited by 107
Evidence for a natural gene transfer from the ponyfish to its bioluminescent bacterial symbiont Photobacter leiognathi. The close relationship between bacteriocuprein and the copper-zinc superoxide dismutase of teleost fishes.
Martin, J. P., & Fridovich, I. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)69131-3 · Cited by 107
Self-citation
Decreased defence against free radicals in rat heart during normal reperfusion after hypoxic, ischemic and calcium-free perfusion
Julicher, R. H. M., Tijburg, L. B. M., Sterrenberg, L., Bast, A., Koomen, J. M., & Noordhoek, J. (1984) · Life Sciences · doi:10.1016/0024-3205(84)90099-7 · Cited by 107
Microbial Gas Metabolism
Cole, J. A. (1976) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/s0065-2911(08)60226-x · Cited by 107
Changes in superoxide dismutase mRNA expression by streptozotocin‐induced diabetes
Kamata, K., & Kobayashi, T. (1996) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.1996.tb15712.x · Cited by 105
Current methods in quantifying ROS and oxidative damage in Caenorhabditis elegans and other model organism of aging
Labuschagne, C. F., & Brenkman, A. B. (2013) · Ageing Research Reviews · doi:10.1016/j.arr.2013.09.003 · Cited by 106
Superoxide Release by Zymosan‐Stimulated Rat Kupffer Cells in vitro
Bhatnagar, R., SCHIRMER, R., Ernst, M., & Decker, K. (1981) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1981.tb05590.x · Cited by 103
Sequence Homologies Among Bacterial and Mitochondrial Superoxide Dismutases
Steinman, H. M., & Hill, R. L. (1973) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.70.12.3725 · Cited by 103
A method for distinguishing Cu,Zn- and Mn-containing superoxide dismutases
Geller, B. L., & Winge, D. R. (1983) · Analytical Biochemistry · doi:10.1016/0003-2697(83)90348-2 · Cited by 102
Higher Oxidation State Manganese Biomolecules
Vincent, J. B., & Christou, G. (1989) · Advances in inorganic chemistry · doi:10.1016/s0898-8838(08)60196-8 · Cited by 102
Overexpression of copper/zinc superoxide dismutase does not prevent neonatal lethality in mutant mice that lack manganese superoxide dismutase
Copin, J., Gasche, Y., & Chan, P. H. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00280-x · Cited by 106
The effects of some antioxidant vitamin‐ and trace element‐supplemented diets on activities of SOD, CAT, GSH‐Px and LPO levels in chicken tissues
Ürek, R. Ö., Bozkaya, L. A., & Tarhan, L. (2001) · Cell Biochemistry and Function · doi:10.1002/cbf.905 · Cited by 100
Salt stress‐induced changes in superoxide dismutase isozymes in leaves and mesophyll protoplasts from Vigna unguiculata (L.) Walp.
Hernández, J. A., del Río, L. A., & Sevilla, F. (1994) · New Phytologist · doi:10.1111/j.1469-8137.1994.tb07527.x · Cited by 99
Developmental Expression and Intracellular Localization of Superoxide Dismutases in Maize* *Research supported by National Institutes of Health Grant No. GM 2273362 (to J.G.S.) and by N.I.H. Training Grant No. 5T01-GM296-18
Baum, J. A., & Scandalios, J. G. (1979) · Differentiation · doi:10.1111/j.1432-0436.1979.tb01576.x · Cited by 100
DPI induces mitochondrial superoxide-mediated apoptosis
Li, N., Ragheb, K., Lawler, G., Sturgis, J., Rajwa, B. P., Melendez, J. A., & Robinson, J. P. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01325-4 · Cited by 98
The chemistry of biological manganese
Lawrence, G. D., & Sawyer, D. T. (1978) · Coordination Chemistry Reviews · doi:10.1016/s0010-8545(00)80358-6 · Cited by 99
Superoxide Dismutase in the Anaerobic Flagellates, Tritrichomonas foetus and Monocercomonas sp
Lindmark, D. G., & Müller, M. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42465-4 · Cited by 99
Assignment of the gene for cytoplasmic superoxide dismutase ( Sod-1 ) to a region of chromosome 16 and of Hprt to a region of the X chromosome in the mouse
Francke, U., & Taggart, R. T. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.10.5230 · Cited by 99
Pathological Conditions Involving Extracellular Hemoglobin: Molecular Mechanisms, Clinical Significance, and Novel Therapeutic Opportunities for α 1 -Microglobulin
Olsson, M. G., Allhorn, M., Bülow, L., Hansson, S. R., Ley, D., Olsson, M. L., Schmidtchen, A., & Åkerström, B. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4282 · Cited by 100
RelB regulates manganese superoxide dismutase gene and resistance to ionizing radiation of prostate cancer cells
Josson, S., Xu, Y., Fang, F., Dhar, S. K., Clair, D. K. S., & Clair, W. H. S. (2005) · Oncogene · doi:10.1038/sj.onc.1209186 · Cited by 97
Particle‐Bound Enzymes in the Bloodstream Form of Trypanosoma brucei
Opperdoes, F. R., Borst, P., & Spits, H. (1977) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1977.tb11566.x · Cited by 97

Authors: Weisiger, R. A., & Fridovich, I.
Affiliations: Duke Medical Center (US)
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1973-05
Volume: 248
Issue: 10
Pages: 3582-3592
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1016/s0021-9258(19)43969-0
OpenAlex: W1580575515
Cited by: 895
References: 37
Citations by year: 2026: 4 · 2025: 8 · 2024: 7 · 2023: 10 · 2022: 11 · 2021: 19 · 2020: 20 · 2019: 18 · 2018: 15 · 2017: 13 · 2016: 9 · 2015: 12 · 2014: 25 · 2013: 13 · 2012: 23
FWCI: 35.05
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 17333 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Topics: Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Keywords: superoxide dismutase, chicken liver, mitochondrial superoxide dismutase, cytosolic superoxide dismutase, manganese superoxide dismutase, copper-zinc superoxide dismutase, enzyme purification, enzyme inactivation, cyanide inhibition, endosymbiotic origin of mitochondria, autoreduction, porcine heart
MeSH terms: Amino Acids, Animals, Chickens, Copper, Cytoplasm, Cytosol, Electrophoresis, Disc, Isoelectric Focusing, Liver, Manganese, Mitochondria, Liver, Molecular Weight, Myocardium, Oxidation-Reduction, Oxidoreductases, Species Specificity, Superoxide Dismutase, Swine, Ultracentrifugation, Zinc

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Superoxide Dismutase

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks